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Structure of CTATM1 in the inward-facing partially occluded with cargo bound

Analyse Structure of CTATM1 in the inward-facing partially occluded with cargo bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PRU
Type: protein
Length: 1,164 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative iron-sulfur protein
UniProt: G0SBE6
Ligands: GSH
Pockets: 15 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 62% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative iron-sulfur protein	protein	582	62% helix, 10% strand	G0SBE6

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	940	0.84	0.86	103	GSH
2	55	0.73	0.98	21	empty
3	50	0.70	0.97	20	empty
4	233	0.58	0.78	39	empty
5	149	0.55	0.81	17	empty

Interfaces

1 interface between chains.

A–B · 6008 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

7PRU · Structure of CtAtm1 in the inward-facing partially occluded with cargo bound · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt G0SBE6
Elsewhere: RCSB PDB 7PRU · PDBe 7PRU · UniProt G0SBE6

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